Prior exercise increases phosphorylation of Akt substrate of 160 kDa (AS160) in rat skeletal muscle

Arias, Edward B.; Kim, Junghoon; Funai, Katsuhiko; Cartee, Gregory D.

doi:10.1152/ajpendo.00602.2006

Cited by 118Metabolism, Diabetes, and CancerMuscle metabolism and nutritionCardiovascular and exercise physiology

Prior exercise increases phosphorylation of Akt substrate of 160 kDa (AS160) in rat skeletal muscle

Arias, Edward B., Kim, Junghoon, Funai, Katsuhiko, Cartee, Gregory D.·2007·American Journal of Physiology-Endocrinology and Metabolism

DOI 10.1152/ajpendo.00602.2006

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Abstract

The main purpose of this study was to determine whether the increased glucose transport (GT) found immediately postexercise (IPEX) or 4 h postexercise (4hPEX) is accompanied by increased phosphorylation of Akt substrate of 160 kDa (AS160, a protein regulator of GLUT4 translocation). Paired epitrochlearis muscles were dissected from rats (sedentary or IPEX, 2-h swim) and used to measure protein phosphorylation and insulin-independent GT. IPEX values exceeded sedentary values for GT and phosphorylations of AS160, AMP-activated protein kinase (pAMPK) and acetyl-CoA carboxylase (pACC) but not for AS160 abundance or phosphorylation of Akt serine (pSerAkt), Akt threonine (pThrAkt), or glycogen synthase kinase-3 (pGSK3). AS160 phosphorylation was significantly correlated with GT ( R = 0.801, P < 0.01) and pAMPK ( R = 0.655, P < 0.05). Muscles from other rats were studied 4hPEX along with sedentary controls. One muscle per rat was incubated without insulin, and the contralateral muscle was incubated with insulin. 4hPEX values exceeded sedentary values for insulin-stimulated GT. The elevated pAMPK and pACC found IPEX had reversed by 4hPEX. Insulin caused a significant increase in pSerAkt, pThrAkt, pGSK3, and AS160 phosphorylation with or without exercise. Exercise significantly increased AS160 phosphorylation, regardless of insulin, with unchanged AS160 abundance. Among the signaling proteins studied, insulin-stimulated GT was significantly correlated only with insulin-stimulated pThrAkt ( R = 0.720, P < 0.0005). The results are consistent with a role for increased AS160 phosphorylation in the increased insulin-independent GT IPEX, and the exercise effects on AS160 phosphorylation and/or pThrAkt at 4hPEX are potentially relevant to the increased insulin-stimulated glucose transport at this time.

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TBC1D4 PAS phosphorylation was elevated in rat skeletal muscle following an acute bout of exercise, an effect that persisted for 3 to 4 hours postexercise.
“Arias et al. [122], was one of the first to show that TBC1D4 PAS phosphorylation was elevated in rat skeletal muscle following an acute bout of exercise, an effect that persisted for 3 to 4 hours postexercise.”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [122]

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AS160 expression, but not AS160 Serine‐588, Threonine‐642, and Serine‐704 phosphorylation, is essential for elevated insulin‐stimulated glucose uptake by skeletal muscle from female rats after acute exercise
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Exercise effects on γ3-AMPK activity, phosphorylation of Akt2 and AS160, and insulin-stimulated glucose uptake in insulin-resistant rat skeletal muscle
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Nitric oxide is required for the insulin sensitizing effects of contraction in mouse skeletal muscle
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Fiber type-specific effects of acute exercise on insulin-stimulated AS160 phosphorylation in insulin-resistant rat skeletal muscle
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Effects of Nutrient Intake Timing on Post-Exercise Glycogen Accumulation and Its Related Signaling Pathways in Mouse Skeletal Muscle
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Roux-en-Y gastric bypass surgery enhances contraction-mediated glucose metabolism in primary human myotubes
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Exercise Intervention on Blood Glucose Control of Type 2 Diabetes with Obesity : A Systematic Review
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A novel genetic model provides a unique perspective on the relationship between postexercise glycogen concentration and increases in the abundance of key metabolic proteins after acute exercise
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Postexercise ketone monoester administration concomitant with glucose stimulates glycogen repletion in soleus muscle in mice
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Effects of Prior Exercise on Insulin-stimulated AS160 Phosphorylation and Glucose Transport in Rat Skeletal Muscle
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Increased AS160 phosphorylation, but not TBC1D1 phosphorylation, with increased postexercise insulin sensitivity in rat skeletal muscle
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Role of Akt substrate of 160 kDa in insulin-stimulated and contraction-stimulated glucose transport
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Sustained postexercise increases in AS160 Thr642and Ser588phosphorylation in skeletal muscle without sustained increases in kinase phosphorylation
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AS160 expression, but not AS160 Serine‐588, Threonine‐642, and Serine‐704 phosphorylation, is essential for elevated insulin‐stimulated glucose uptake by skeletal muscle from female rats after acute exercise
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Authors: Arias, E. B., Kim, J., Funai, K., & Cartee, G. D.
Affiliations: University of Michigan (US)
ORCID: Arias, Edward B.
Funai, Katsuhiko
Cartee, Gregory D.
Venue: American Journal of Physiology-Endocrinology and Metabolism
Publisher: American Physiological Society
Published: 2007-04
Volume: 292
Issue: 4
Pages: E1191-E1200
ISSN: 0193-1849 (ISSN-L)
1522-1555
DOI: 10.1152/ajpendo.00602.2006
OpenAlex: W2145108000
Cited by: 118
References: 50
Citations by year: 2025: 2 · 2024: 2 · 2023: 3 · 2022: 2 · 2021: 6 · 2020: 7 · 2019: 14 · 2018: 7 · 2017: 4 · 2016: 10 · 2015: 7 · 2014: 8 · 2013: 4 · 2012: 5
FWCI: 2.86
Type: journal article
Language: en
Open access: closed
Locations: American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (AG 10026)
National Institute of Diabetes and Digestive and Kidney Diseases (DK071771, R01DK071771)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
Health Sciences › Medicine › Complementary and alternative medicine › Cardiovascular and exercise physiology
Keywords: AS160, protein phosphorylation, skeletal muscle, physical activity, glucose transport, GLUT4 translocation, AMPK, acetyl-CoA carboxylase, glycogen synthase kinase-3, insulin-independent glucose transport, insulin-stimulated glucose transport, epitrochlearis muscle, swimming training
MeSH terms: Acetyl-CoA Carboxylase, Animals, Biological Transport, Glucose, Insulin, Male, Molecular Weight, Multienzyme Complexes, Phosphorylation, Physical Conditioning, Animal, Substrate Specificity, Swimming, Time Factors, Rats, Wistar, Protein Serine-Threonine Kinases, Muscle, Skeletal, 3-O-Methylglucose, Glycogen Synthase Kinase 3, Proto-Oncogene Proteins c-akt, Rats, AMP-Activated Protein Kinases

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Prior exercise increases phosphorylation of Akt substrate of 160 kDa (AS160) in rat skeletal muscle

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